1980 Volume 13 Issue 5 Pages 486-498
The immunohistochemical localization of hen egg-white proteins, ovalbumin, lysozyme and ovomucoid, was investigated by means of the fluorescein and enzyme-labeled antibody technique, using the new GMA-Quetol 523-instead of the conventional paraffin embedding method. This method is simpler than paraffin embedding because the embedding matrix need not be removed. Also, it is easy to cut 1-2μm sections with glass knives on a JB-4 microtome. The distribution pattern of each protein could be observed far more precisely than with paraffin sections. The three proteins showed different secretory features, depending on the stage of the ovulation cycle. Ovalbumin was secreted into the oviduct lumen prior to the descent of the egg. While the ovum with a completely calcified shell remained in the uterus, the tubular gland cells were filled with immuno-positive small granules. This was thought to represent the synthesizing stage of ovalbumin in preparation for the next ovulation. Lysozyme was secreted before and after the descent of the egg. When the complete egg was located in the uterus, the immunopositive lysozyme could not be detected in any region of the oviduct. Ovomucoid was also secreted prior to the descent of the egg.